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Ligand maltopentaose

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (6 results)

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Show Natural Substrate (6 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.4.1.25

maltopentaose + maltopentaose = maltooligosaccharides

489019, 489001, 489002, 489011, 488995, 489005

-

2.4.1.4

sucrose + maltopentaose = D-fructose + maltohexaose

735805

-

3.2.1.1

maltopentaose + H2O = malto-oligomers + maltose

666785

-

3.2.1.1

maltopentaose + H2O = maltose + D-glucose + ?

701883

-

3.2.1.1

2 entries

3.2.1.98

maltopentaose + H2O = ?

731665

-

3.2.1.B8

maltopentaose + H2O = maltose + D-glucose + ?

707349

-

In Vivo Product in Enzyme-catalyzed Reactions (5 results)

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Show Natural Product (5 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.4.1.4

sucrose + maltotetraose = D-fructose + maltopentaose

0

-

3.2.1.1

3 glycogen = maltotriose + maltotetraose + maltopentaose

0

-

3.2.1.1

amylose + H2O = maltotriose + maltotetraose + maltopentaose

0

-

3.2.1.1

starch + H2O = maltohexaose + maltopentaose + maltotriose

0

-

3.2.1.1

starch + H2O = maltotriose + maltotetraose + maltopentaose

0

-

3.2.1.1

4 entries

Substrate in Enzyme-catalyzed Reactions (95 results)

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Show Substrate (95 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.99.B3

maltopentaose + O2 = ?

685689

-

2.3.1.79

acetyl-CoA + maltopentaose = CoA + 6-O-acetyl-alpha-D-glucopyranosyl-(1->4)-alpha-D-glucopyranosyl-(1->4)-alpha-D-glucopyranosyl-(1->4)-alpha-D-glucopyranosyl-(1->4)-D-glucopyranose

487512

-

2.4.1.1

maltopentaose + alpha-D-glucose 1-phosphate = maltohexaose + phosphate

658355, 659735, 701969

-

2.4.1.1

maltopentaose + glucose 1-phosphate = maltohexaose + phosphate

488254, 488265, 488264, 488256, 488295, 488262, 488261

-

2.4.1.1

maltopentaose + phosphate = ?

686672

-

2.4.1.1

maltopentaose + phosphate = maltotetraose + alpha-D-glucose 1-phosphate

702452, 657863, 701969

-

2.4.1.1

4 entries

2.4.1.11

UDP-glucose + maltopentaose = ? + UDP

488405

-

2.4.1.162

sucrose + maltopentaose = D-glucose + beta-D-fructofuranosyl-(2,1)-maltopentaoside

692116

-

2.4.1.162

sucrose + maltopentaose = D-glucose + beta-D-fructofuranosyl-(2->1)-maltopentaoside

488677

-

2.4.1.162

2 entries

2.4.1.18

maltopentaose = ?

705085

-

2.4.1.19

maltopentaose + glycosyl acceptor = beta-cyclodextrin

488834

-

2.4.1.19

maltopentaose + L-ascorbic acid = 2-O-alpha-D-glucopyranosyl-L-ascorbic acid

756523

-

2.4.1.19

2 entries

2.4.1.2

maltopentaose = dextran

488882, 488876

-

2.4.1.21

ADP-alpha-D-glucose + maltopentaose = ADP + maltohexaose

736158, 735356, 737088

-

2.4.1.21

ADP-glucose + maltopentaose = ADP + maltohexaose

488926

-

2.4.1.248

maltopentaose = ?

759621

-

2.4.1.248

maltopentaose = cyclo-(-6)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-) + ?

698519

-

2.4.1.25

amylopectin + maltopentaose = maltooligosaccharides

489014, 489012, 489005, 489007

-

2.4.1.25

amylose + maltopentaose = cyclic alpha-1,4-glucan

489022, 489007, 489016, 489019, 489010, 489015

-

2.4.1.25

amylose + maltopentaose = maltooligosaccharides

489012, 489005, 489007

-

2.4.1.25

maltoheptaose + maltopentaose = maltooligosaccharides

489000, 489010, 488995, 489005

-

2.4.1.25

maltohexaose + maltopentaose = maltooligosaccharides

488997, 488995, 489005

-

2.4.1.25

maltopentaose + glycosyl acceptor = maltose + D-glucose + maltooligosaccharides

755942, 755955

-

2.4.1.25

maltopentaose + maltodextrin = maltose + higher dextrins

488998

-

2.4.1.25

maltopentaose + maltopentaose = ?

685153

-

2.4.1.25

maltopentaose + maltopentaose = D-glucose + maltooligosaccharides

660766

-

2.4.1.25

maltopentaose + maltopentaose = maltooligosaccharides

736255, 662665, 489019, 489001, 489002, 489011, 488995, 489005

-

2.4.1.25

maltopentaose + maltopentaose = new oligosaccharides

488995, 489005, 489010

-

2.4.1.25

maltopentaose + maltotriose = D-glucose + maltooligosaccharides

489011, 489007

-

2.4.1.25

maltopentaose + maltotriose = homologous 1,4-alpha-D-glucans

488998

-

2.4.1.25

maltopentaose + maltotriose = maltodextrins

489011, 489001

-

2.4.1.25

maltopentaose + maltotriose = maltoheptaose + D-glucose

488998

-

2.4.1.25

maltotetraose + maltopentaose = maltooligosaccharides

489010, 489000, 489005, 489007

-

2.4.1.25

starch + maltopentaose = alpha-1,4-D-glucans

488995, 489005, 489012, 489007

-

2.4.1.21

2 entries

2.4.1.248

2 entries

2.4.1.25

17 entries

2.4.1.387

maltopentaose = cyclo-[(->6)-alpha-D-Glcp-(1->3)-alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->3)-alpha-D-Glcp-(1->)]

764316

-

2.4.1.4

sucrose + maltopentaose = D-fructose + maltohexaose

735805

-

2.4.1.4

sucrose + maltopentaose = D-fructose + maltohexaose + maltoheptaose

489140

-

2.4.1.B34

amylose V + maltopentaose = ?

760023

-

2.4.1.B34

maltopentaose + H2O = ?

760023

-

2.4.1.B34

maltopentaose + H2O = D-glucose + maltotetraose

721349

-

2.4.1.B34

maltopentaose = ?

735514, 735534, 735717

-

2.4.1.4

2 entries

2.4.1.B34

4 entries

2.4.99.B5

acarbose + maltopentaose = acarviosyl-(1->4)-alpha-maltopentaose + maltose

729911

-

3.2.1.1

maltodextrin G5 + H2O = maltodextrin G2 + maltodextrin G3

664980

-

3.2.1.1

maltopentaose + H2O = ?

678813, 665013

-

3.2.1.1

maltopentaose + H2O = D-glucose + maltose + ?

752105

-

3.2.1.1

maltopentaose + H2O = glucose + maltose + maltotriose

678799

-

3.2.1.1

maltopentaose + H2O = malto-oligomers + maltose

666785

-

3.2.1.1

maltopentaose + H2O = maltose + ?

750815

-

3.2.1.1

maltopentaose + H2O = maltose + D-glucose + ?

701883

-

3.2.1.1

maltopentaose + H2O = maltose + maltotriose

729090

-

3.2.1.1

maltopentaose + H2O = maltotetraose + maltotriose + maltose

655083

-

3.2.1.1

maltopentaose + H2O = maltotetraose + maltotriose + maltose + D-glucose

693604

-

3.2.1.1

maltopentaose + H2O = maltotriose + maltose

654643

-

3.2.1.1

maltopentaose + H2O = maltotriose + maltose + D-glucose

750815

-

3.2.1.1

maltopentaose + H2O = more

393379, 393367, 393450, 136189, 393365, 393462, 393426, 393431

-

3.2.1.10

maltopentaose + H2O = ?

654808

-

3.2.1.10

maltopentose + H2O = ?

693790

-

3.2.1.1

13 entries

3.2.1.10

2 entries

3.2.1.106

maltopentaose = ?

699548

-

3.2.1.116

maltopentaose + H2O = maltotriose + D-maltose

731585, 646647, 646648

-

3.2.1.116

maltopentaose + H2O = maltotriose + maltose

749728

-

3.2.1.133

maltopentaose + H2O = 2 maltose + D-glucose

727388

-

3.2.1.133

maltopentaose + H2O = ?

664208

-

3.2.1.133

maltopentaose + H2O = alpha-maltose + ?

678461

-

3.2.1.133

maltopentaose + H2O = maltose + D-glucose + ?

724097

-

3.2.1.135

maltopentaose + H2O = ?

703502

-

3.2.1.135

maltopentaose + H2O = D-glucose + maltose + ?

646816, 393353

-

3.2.1.116

2 entries

3.2.1.133

4 entries

3.2.1.135

2 entries

3.2.1.141

maltopentaose + H2O = ?

692727, 680283

-

3.2.1.2

maltopentaose + H2O = 2 maltose + D-glucose

666019, 727388

-

3.2.1.2

maltopentaose + H2O = ?

208638, 208643, 208642, 656955, 655918, 655912, 655927, 654708

-

3.2.1.2

maltopentose + H2O = ?

656678

-

3.2.1.20

maltopentaose + 4 H2O = 5 alpha-D-glucose

661611

-

3.2.1.20

maltopentaose + H2O = ?

717984, 678787, 722938

-

3.2.1.20

maltopentaose + H2O = alpha-D-glucose + ?

393337, 393350, 393325, 393260, 393340, 393334, 656390, 393348, 655000, 393319, 393261, 393353, 393356, 393341, 678787, 680469, 725283

-

3.2.1.20

maltopentaose + H2O = beta-maltose + maltotriose

393282

-

3.2.1.20

maltopentaose + H2O = D-glucose + ?

657123, 655050, 654259, 655023, 748424, 656703, 709498, 708224

-

3.2.1.3

maltopentaose + 4 H2O = 5 beta-D-glucose

728944

-

3.2.1.3

maltopentaose + H2O = ?

693790, 136187, 136194, 136199, 136242, 136196, 136184, 136228, 136231, 136240, 136241, 136223, 136189, 750105

-

3.2.1.3

maltopentaose + H2O = D-glucose + ?

707265

-

3.2.1.3

maltopentaose + H2O = maltotetraose + beta-D-glucose

677784, 663981, 717106, 654806, 678808, 664362, 665013

-

3.2.1.2

3 entries

3.2.1.20

5 entries

3.2.1.3

4 entries

3.2.1.41

maltopentaose + H2O = maltotriose + maltose

136429, 136432, 136427

-

3.2.1.48

maltopentaose + H2O = ?

136516

-

3.2.1.54

maltopentaose + H2O = ?

664779

-

3.2.1.54

maltopentaose + H2O = D-glucose + maltose + ?

665437

-

3.2.1.54

maltopentaose + H2O = maltose + D-glucose + ?

707248

-

3.2.1.54

maltopentaose + H2O = maltose + maltotriose

136617, 136620, 136609, 136613, 136615, 136611, 136618

-

3.2.1.54

4 entries

3.2.1.60

maltopentaose + H2O = ?

136738

-

3.2.1.68

maltopentaose + H2O = ?

136800

-

3.2.1.98

maltopentaose + H2O = ?

731665

-

3.2.1.B36

maltopentaose + H2O = 2 maltose + D-glucose

724097, 727388

-

3.2.1.B8

malto-pentaose + H2O = maltose + D-glucose

707349

-

3.2.1.B8

maltopentaose + H2O = maltose + D-glucose + ?

707349

-

3.2.1.B8

2 entries

4.2.2.13

maltopentaose = ?

650299

-

5.4.99.15

maltopentaose = ?

651359, 724886

-

5.4.99.15

Maltopentaose = alpha-Maltotriosyl trehalose

3488, 3486, 3487, 680274, 680309, 681347, 724948, 724886

-

5.4.99.15

maltopentaose = alpha-maltotriosyltrehalose

721858, 722996

-

5.4.99.15

3 entries

Product in Enzyme-catalyzed Reactions (63 results)

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Show Product (63 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.4.1.1

maltohexaose + arsenate = maltopentaose + glucose 1-arsenate

488295

-

2.4.1.1

maltohexaose + phosphate = maltopentaose + alpha-D-glucose 1-phosphate

0

-

2.4.1.1

maltotetraose + alpha-D-glucose 1-phosphate = maltopentaose + phosphate

0

-

2.4.1.1

maltotetraose + D-glucose-1-phosphate = maltopentaose + phosphate

0

-

2.4.1.1

maltotetraose + glucose 1-phosphate = maltopentaose + phosphate

488294, 488254, 488264, 488295, 0, 488256, 488239, 488262, 488297

-

2.4.1.19

maltotriose + maltotetraose = maltopentaose

488839

-

2.4.1.19

soluble starch + glycosyl acceptor = maltose + maltotriose + maltotetraose + maltopentaose

488862

-

2.4.1.1

5 entries

2.4.1.19

2 entries

2.4.1.21

ADP-alpha-D-glucose + maltotetraose = ADP + maltopentaose

0

-

2.4.1.25

maltohexaose + maltodextrin = D-glucose + maltopentaose

488998

-

2.4.1.25

maltotriose + glycosyl acceptor = D-glucose + maltose + maltotetraose + maltopentaose + maltohexaose

489010

-

2.4.1.25

maltotriose + maltodextrin = maltopentaose + ?

488998

-

2.4.1.25

maltotriose + maltotriose = D-glucose + maltopentaose

0

-

2.4.1.25

maltotriose + maltotriose = D-glucose + maltopentaose + maltoheptaose + maltononaose + maltoundecaose

488998

-

2.4.1.25

maltotriose + maltotriose = maltopentaose + D-glucose

489001, 489000, 489004, 488998

-

2.4.1.25

maltotriose + maltotriose = maltopentaose + maltotetraose

489020, 488997, 489010

-

2.4.1.25

7 entries

2.4.1.387

2 alpha-isomaltosyl-(1->4)-maltopentaose = cycloalternan + 2 maltopentaose

0

-

2.4.1.4

sucrose + maltotetraose = D-fructose + maltopentaose

0

-

2.4.1.B34

maltohexaose + H2O = D-glucose + maltopentaose

0

-

3.2.1.1

4-nitrophenyl alpha-D-maltopentaoside + H2O = 4-nitrophenol + alpha-D-maltopentaose

0

-

3.2.1.1

4-nitrophenyl-alpha-D-maltopentaoside + H2O = 4-nitrophenol + alpha-D-maltopentaose

0

-

3.2.1.1

4-nitrophenyl-alpha-D-maltopentaoside + H2O = 4-nitrophenol + alpha-D-maltopentaoside

0

-

3.2.1.1

3 glycogen = maltotriose + maltotetraose + maltopentaose

0

-

3.2.1.1

amylose + H2O = maltotriose + maltotetraose + maltopentaose

0

-

3.2.1.1

corn starch + H2O = maltohexaose + maltopentaose + maltotriose

0

-

3.2.1.1

gelatinized starch + H2O = maltotetraose + maltopentaose + maltohexaose

0

-

3.2.1.1

maltoheptaose + H2O = maltohexaose + maltopentaose + maltotetraose + maltotriose + maltose

0

-

3.2.1.1

maltohexaose + H2O = maltopentaose + maltotetraose + maltotriose + maltose

0

-

3.2.1.1

maltooligosaccharides + H2O = maltohexaose + maltopentaose + maltotetraose + maltotriose + maltose

0

-

3.2.1.1

maltotriose = maltose + glucose + maltotetraose + maltopentaose + maltohexaose

393429

-

3.2.1.1

potato starch + H2O = maltohexaose + maltopentaose + maltotriose

0

-

3.2.1.1

soluble potato starch + H2O = maltopentaose + maltose + maltotriose

0

-

3.2.1.1

starch + H2O = maltohexaose + maltopentaose + maltotriose

0

-

3.2.1.1

starch + H2O = maltotriose + maltotetraose + maltopentaose

0

-

3.2.1.1

wheat starch + H2O = maltohexaose + maltopentaose + maltotriose

0

-

3.2.1.135

amylose + H2O = maltotriose + maltotetraose + maltopentaose

0

-

3.2.1.135

pullulan + H2O = maltotriose + maltopentaose + maltohexaose + maltoheptaose

0

-

3.2.1.135

soluble and raw starch + H2O = maltose + maltotriose + maltotetraose + maltopentaose + maltohexaose + maltoheptaose + ?

0

-

3.2.1.141

maltopentaosyltrehalose + H2O = maltopentaose + alpha,alpha'-trehalose

0

-

3.2.1.141

maltosylpentaosyltrehalose + H2O = trehalose + maltopentaose

0

-

3.2.1.1

16 entries

3.2.1.135

3 entries

3.2.1.141

2 entries

3.2.1.142

limit dextrin + H2O = maltotriose + maltotetraose + maltopentaose

0

-

3.2.1.196

beta-cyclodextrin-alpha-1,6-linked maltopentaose + H2O = beta-cyclodextrin + maltopentaose

0

-

3.2.1.2

4-nitrophenyl maltopentaose + H2O = 4-nitrophenol + maltopentaose

0

-

3.2.1.2

p-nitrophenylmaltopentaoside + H2O = p-nitrophenol + maltopentaose

0

-

3.2.1.20

maltoheptaose + H2O = beta-maltose + maltopentaose

0

-

3.2.1.20

maltohexaose + H2O = maltopentaose + D-glucose

0, 393353

-

3.2.1.2

2 entries

3.2.1.20

2 entries

3.2.1.207

maltohexaose + H2O = maltopentaose + D-glucose

0

-

3.2.1.3

maltohexaose + H2O = maltopentaose + D-glucose

0

-

3.2.1.33

63-alpha-glucosyl maltopentaose + H2O = maltopentaose + D-glucose

171378

-

3.2.1.41

amylopectin + H2O = maltohexaose + maltopentaose + maltotetraose + maltotriose + maltose + D-glucose

0

-

3.2.1.41

amylopectin + H2O = maltotriose + maltotetraose + maltopentaose + maltohexaose

0

-

3.2.1.41

starch + H2O = maltohexaose + maltopentaose + maltotetraose + maltotriose + maltose + D-glucose

0

-

3.2.1.54

4-nitrophenyl-alpha-D-maltopentaoside + H2O = 4-nitrophenol + alpha-D-maltopentaoside

0

-

3.2.1.54

beta-cyclodextrin + H2O = maltose + maltotriose + maltotetraose + maltopentaose + maltoheptaose + glucose

0, 136615

-

3.2.1.54

gamma-cyclodextrin + H2O = glucose + maltose + maltotriose + maltotetraose + maltopentaose + maltohexaose + maltoheptaose + maltooctaose

0, 136619

-

3.2.1.54

p-nitrophenyl-D-maltopentaoside + H2O = p-nitrophenol + maltopentaose

0

-

3.2.1.41

3 entries

3.2.1.54

4 entries

3.2.1.60

4-nitrophenyl-maltopentaoside + H2O = 4-nitrophenol + maltopentaose

0

-

3.2.1.98

maltoheptaose + H2O = maltohexaose + maltotriose + maltotetraose + maltopentaose + maltose + D-glucose

0

-

3.2.1.98

maltohexaose + H2O = D-glucose + maltopentaose

0, 171735, 171733, 171736

-

3.2.1.98

soluble starch + H2O = maltohexaose + maltopentaose + maltose + D-glucose + maltotriose + maltotetraose

0

-

3.2.1.98

starch + H2O = maltohexaose + maltopentaose

0

-

3.2.1.B8

4-nitrophenyl alpha-maltopentaoside + H2O = maltopentaose + 4-nitrophenol

0

-

3.2.1.B8

4-nitrophenyl alpha-maltopentaoside = maltopentaose + 4-nitrophenol

0

-

3.2.1.98

4 entries

3.2.1.B8

2 entries

5.4.99.15

alpha-maltotriosyl trehalose = maltopentaose

649108

-

Activator in Enzyme-catalyzed Reactions (2 results)

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Show Activating Compound (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.4.1.25

stimulating effect of maltooligosaccharides on the conversion of amylose, 15 mM, relative activity 210%

489005

-

3.2.1.33

20 mM: 1.45fold activation

171381

-

Inhibitor in Enzyme-catalyzed Reactions (2 results)

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Show Inhibitors (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

3.2.1.1

30 mM, 51% inhibition

656677

-

3.2.1.3

-

728944

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (75 results)

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Show Turnover Number (75 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.99.B3

0.9

-

2,6-dichlorophenol indophenol used as electron acceptor

685689

1.1.99.B3

1.8

-

O2 used as electron acceptor

685689

2.4.1.1

0.033

-

pH 7.0

686672

2.4.1.1

2.2

-

pH 6.5, 37°C, recombinant enzyme, phosphorolysis reaction

659735

2.4.1.1

5.4

-

pH 6.5, 37°C, recombinant enzyme, synthesis reaction

659735

2.4.1.1

33.8

-

phosphorolysis

488295

2.4.1.25

0.025

-

mutant enzyme N287Y, at pH 6.0 and 30°C

755942

2.4.1.25

3.98

-

pH 5.5, 70°C, mutant D249S

685153

2.4.1.25

4.8

-

wild type enzyme, at pH 6.0 and 30°C

755942

2.4.1.25

22

-

pH 6.6, 70°C

662665

2.4.1.25

24.8

-

pH 6.7, 80°C

660766

2.4.1.25

179

-

pH 5.5, 70°C, mutant F366L

685153

2.4.1.25

329

-

pH 5.5, 70°C, wild-type enzyme

685153

2.4.1.4

47

-

pH 7.0, 30°C, recombinant wild-type enzyme

735805

2.4.1.4

173

-

pH 7.0, 30°C, recombinant mutant R226N

735805

3.2.1.1

37.2

-

pH 5.6, 40°C

678813

3.2.1.1

94.7

-

-

136189

3.2.1.1

283

-

in 50 mM sodium phosphate buffer (pH 6.5) at 75°C

701883

3.2.1.1

567.01

-

pH 6.5, 40°C, recombinant enzyme

752105

3.2.1.1

754

-

-

393462

1.1.99.B3

2 entries

2.4.1.1

4 entries

2.4.1.25

7 entries

2.4.1.4

2 entries

3.2.1.1

5 entries

3.2.1.116

58.1

-

pH 6.0, 37°C

749728

3.2.1.133

0.0017

-

pH 5.0, 90°C

724097

3.2.1.133

3.85

-

pH 5.0, 85°C

727388

3.2.1.133

69.01

-

50°C, pH 6.0, mutant enzyme A290I

664208

3.2.1.133

197

-

50°C, pH 6.0, wild-type enzyme

664208

3.2.1.141

14.4

-

mutant enzyme Y328F, 60°C, 50 mM citrate phosphate buffer, pH 5

692727

3.2.1.141

15.5

-

mutant enzyme R356K, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation

692727

3.2.1.141

17.4

-

mutant enzyme A259S, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation

692727

3.2.1.141

17.7

-

-

680283

3.2.1.141

17.7

-

wild-type enzyme, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation

692727

3.2.1.141

19.1

-

mutant enzyme F355Y, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation

692727

3.2.1.2

0.034

-

pH 5.4, 37°C, mutant E380Q

666019

3.2.1.2

0.08

-

pH 5.4, 37°C, mutant E186Q

666019

3.2.1.2

3.85

-

pH 5.0, 85°C

727388

3.2.1.2

1280

-

pH 5.4, 37°C, wild-type enzyme

666019

3.2.1.20

0.02

-

pH 4.0, 80°C

722938

3.2.1.20

1.05

-

-

393341

3.2.1.20

7.15

-

-

393334

3.2.1.20

13

-

pH 5.0, 37°C, alpha-glucosidase I

678787

3.2.1.20

15

-

-

678787

3.2.1.20

64.3

-

pH 6.8, 30°C, recombinant enzyme

657123

3.2.1.20

147

-

-

393340

3.2.1.20

316

-

-

709498

3.2.1.20

611

-

pH 5.0, 95°C

725283

3.2.1.20

810

-

pH 4.5, 35°C

661611

3.2.1.3

27.3

-

wild-type enzyme

136228

3.2.1.3

41.1

-

-

136196

3.2.1.3

41.8

-

mutant enzyme S119Y

136241

3.2.1.3

43.8

-

recombinant AmyD, pH 5.5, 40°C

717106

3.2.1.3

44

-

recombinant glucoamylase

654806

3.2.1.3

56.3

-

pH 6.5, 40°C, recombinant enzyme

664362

3.2.1.3

73.7

-

recombinant AmyC, pH 5.5, 40°C

717106

3.2.1.3

122

-

pH 5.0, 40°C

728944

3.2.1.3

518

-

pH 5.0, 75°C

707265

3.2.1.3

800

-

-

136187

3.2.1.B36

0.0017

-

pH 5.0, 90°C

724097

3.2.1.B36

3.85

-

pH 5.0, 85°C

727388

3.2.1.133

4 entries

3.2.1.141

6 entries

3.2.1.2

4 entries

3.2.1.20

10 entries

3.2.1.3

10 entries

3.2.1.B36

2 entries

3.2.1.B8

5.18

-

pH 6.5, 85°C, recombinant enzyme

707349

5.4.99.15

13.4

-

pH 5, 60°C, mutant enzyme R614A

724886

5.4.99.15

13.4

-

pH 5.0, 60°C, mutant enzyme R614A

724886

5.4.99.15

30.2

-

pH 5, 60°C, mutant enzyme D411A

724886

5.4.99.15

30.2

-

pH 5.0, 60°C, mutant enzyme D411A

724886

5.4.99.15

87.2

-

pH 5, 60°C, mutant enzyme D610A

724886

5.4.99.15

87.2

-

pH 5.0, 60°C, mutant enzyme D610A

724886

5.4.99.15

197

-

mutant F405S, pH 5.0, 60°C

680309

5.4.99.15

267

-

mutant Y409F, pH 5.0, 60°C

680274

5.4.99.15

280

-

pH 5.0, 60°C, mutant enzyme P402Q

724886

5.4.99.15

354

-

mutant F405Y, pH 5.0, 60°C

680274, 680309

5.4.99.15

357

-

pH 5.0, 60°C, mutant enzyme V426T

724886

5.4.99.15

364

-

wild-type, pH 5.0, 60°C

680274, 680309

5.4.99.15

410

-

mutant F405W, pH 5.0, 60°C

680309

5.4.99.15

411

-

pH 5, 60°C, wild-type enzyme

724886

5.4.99.15

411

-

pH 5.0, 60°C, wild-type enzyme

724886

5.4.99.15

481

-

mutant F405M, pH 5.0, 60°C

680309

5.4.99.15

530

-

pH 5.0, 60°C, mutant enzyme A406S

724886

5.4.99.15

17 entries

K_M Value (130 results)

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Show KM Value (130 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.99.B3

11

-

2,6-dichlorophenol indophenol used as electron acceptor

685689

1.1.99.B3

32

-

O2 used as electron acceptor

685689

2.4.1.1

0.11

-

-

488254

2.4.1.1

0.17

-

pH 6.5, 37°C, recombinant enzyme, phosphorolysis reaction

659735

2.4.1.1

0.23

-

stromal phosphorylase, phosphorolysis

488304

2.4.1.1

0.27

-

stromal phosphorylase, synthesis

488304

2.4.1.1

0.28

-

pH 6.5, 37°C, recombinant enzyme, synthesis reaction

659735

2.4.1.1

0.49

-

synthesis, isoenzyme P-2

488261

2.4.1.1

0.93

-

phosphorolysis

488256

2.4.1.1

1.7

-

synthesis, isoenzyme P-1

488261

2.4.1.1

2.73

-

phosphorolysis

488295

2.4.1.1

3

-

synthesis

488256

2.4.1.1

3.5

-

pH 7.0, 30°C, recombinant mutant H334A, phosphorolysis

657863

2.4.1.1

3.8

-

pH 7.0, 30°C, recombinant wild-type enzyme, phosphorolysis

657863

2.4.1.1

4.1

-

pH 7.0, 30°C, recombinant mutant H334Q, phosphorolysis

657863

2.4.1.1

8.8

-

-

488254

2.4.1.1

8.8

-

phosphorolysis

488254

2.4.1.1

9.1

-

-

488254

2.4.1.1

9.1

-

phosphorolysis

488254

2.4.1.1

38

-

synthesis

488254

2.4.1.1

42

-

synthesis

488254

2.4.1.1

103

-

pH 7.0, 30°C, recombinant mutant H334N, phosphorolysis

657863

2.4.1.1

280

-

pH 7.0

686672

1.1.99.B3

2 entries

2.4.1.1

21 entries

2.4.1.2

0.0033

-

-

488882

2.4.1.21

46.32

-

isoform GBSSI, at pH 8.5 and 30°C

736158

2.4.1.25

4.2

-

pH 6.6, 70°C

662665

2.4.1.25

6.9

-

pH 6.7, 80°C

660766

2.4.1.25

15.4

-

mutant enzyme N287Y, at pH 6.0 and 30°C

755942

2.4.1.25

18.6

-

wild type enzyme, at pH 6.0 and 30°C

755942

2.4.1.4

0.024

-

pH 7.0, 30°C, recombinant mutant R226N

735805

2.4.1.4

61

-

pH 7.0, 30°C, recombinant wild-type enzyme

735805

3.2.1.1

0.12

-

-

393379

3.2.1.1

0.55

-

pH 5.6, 40°C

678813

3.2.1.1

0.95

-

-

393462

3.2.1.1

1.69

-

in 50 mM sodium phosphate buffer (pH 6.5) at 75°C

701883

3.2.1.1

1.92

-

pH 6.5, 40°C, recombinant enzyme

752105

3.2.1.1

2.7

-

-

393365

3.2.1.1

3.1

-

-

136189

2.4.1.25

4 entries

2.4.1.4

2 entries

3.2.1.1

7 entries

3.2.1.10

3.6

-

IP-SI, immunoprecipitated human sucrase-isomaltase complex

693790

3.2.1.116

37.9

-

pH 6.0, 37°C

749728

3.2.1.133

3.5

-

50°C, pH 6.0, mutant enzyme A290I

664208

3.2.1.133

3.97

-

50°C, pH 6.0, wild-type enzyme

664208

3.2.1.133

4.4

-

kinetic parameters for C14-labelled maltooligosaccharides

678461

3.2.1.133

16.2

-

pH 5.0, 85°C

727388

3.2.1.133

21.2

-

pH 5.0, 90°C

724097

3.2.1.141

5.08

-

mutant enzyme R356K, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation

692727

3.2.1.141

5.37

-

mutant enzyme A259S, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation

692727

3.2.1.141

5.82

-

mutant enzyme Y328F, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation

692727

3.2.1.141

5.86

-

-

680283

3.2.1.141

5.86

-

wild-type enzyme, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation

692727

3.2.1.141

7.74

-

mutant enzyme F355Y, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation

692727

3.2.1.2

1.02

-

-

208642

3.2.1.2

1.94

-

pH 5.4, 37°C, wild-type enzyme

666019

3.2.1.2

2.02

-

pH 5.4, 37°C, mutant E380Q

666019

3.2.1.2

2.15

-

pH 5.4, 37°C, mutant E186Q

666019

3.2.1.2

2.83

-

mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S

208638

3.2.1.2

16.2

-

pH 5.0, 85°C

727388

3.2.1.20

0.14

-

-

393319

3.2.1.20

0.22

-

-

393260

3.2.1.20

0.32

-

pH 5.0, 95°C

725283

3.2.1.20

0.64

-

-

393337

3.2.1.20

0.96

-

pH 5.5, 45°C

654259

3.2.1.20

1

-

alpha-glucosidase I

393261

3.2.1.20

1.5

-

alpha-glucosidase II

393261

3.2.1.20

1.9

-

-

393340

3.2.1.20

2.33

-

pH 4.0, 80°C

722938

3.2.1.20

2.35

-

-

393325

3.2.1.20

2.4

-

-

393282

3.2.1.20

2.6

-

-

393341

3.2.1.20

2.8

-

pH 5.0, 37°C

655023

3.2.1.20

2.92

-

-

393334

3.2.1.20

3.2

-

-

393340

3.2.1.20

3.99

-

-

708224

3.2.1.20

4.7

-

pH 6.8, 30°C, recombinant enzyme

657123

3.2.1.20

5.5

-

-

678787

3.2.1.20

5.5

-

pH 5.0, 37°C, alpha-glucosidase I

678787

3.2.1.20

6.72

-

-

709498

3.2.1.20

8

-

-

393348

3.2.1.20

14

-

pH 4.5, 35°C

661611

3.2.1.20

63

-

pH 5.5, 35°C

655000

3.2.1.3

0.03

-

pH 5.0, 40°C

728944

3.2.1.3

0.05

-

IP-MGAM, immunoprecipitated maltase-glucoamylase

693790

3.2.1.3

0.066

-

glucoamylase G3

136223

3.2.1.3

0.067

-

glucoamylase G4 or G5

136223

3.2.1.3

0.07

-

glucoamylase G1

136223

3.2.1.3

0.071

-

glucoamylase G2

136223

3.2.1.3

0.1

-

recombinant glucoamylase

654806

3.2.1.3

0.1

-

wild-type enzyme

136228

3.2.1.3

0.116

-

-

136184

3.2.1.3

0.12

-

-

136194

3.2.1.3

0.13

-

free enzyme

136242

3.2.1.3

0.14

-

enzyme form GII

136194

3.2.1.3

0.16

-

enzyme form GI

136194

3.2.1.3

0.17

-

enzyme form GIII

136194

3.2.1.3

0.17

-

mutant enzyme S119Y

136241

3.2.1.3

0.224

-

recombinant AmyC, pH 5.5, 40°C

717106

3.2.1.3

0.93

-

recombinant AmyD, pH 5.5, 40°C

717106

3.2.1.3

1.63

-

pH 5.0, 75°C

707265

3.2.1.3

3.94

-

pH 6.5, 40°C, recombinant enzyme

664362

3.2.1.3

4.33

-

-

136187

3.2.1.3

5.1

-

-

136189

3.2.1.3

6.66

-

ntMGAM, N-terminal subunit of MGAM, Vmax: 6.97 U/mg

693790

3.2.1.133

5 entries

3.2.1.141

6 entries

3.2.1.2

6 entries

3.2.1.20

23 entries

3.2.1.3

22 entries

3.2.1.48

13.3

-

-

136516

3.2.1.54

1.2

-

-

136615

3.2.1.54

2.3

-

-

136609

3.2.1.54

2 entries

3.2.1.98

10.02

-

-

171733

3.2.1.B36

16.2

-

pH 5.0, 85°C

727388

3.2.1.B36

21.2

-

pH 5.0, 90°C

724097

3.2.1.B36

2 entries

3.2.1.B8

9.95

-

pH 6.5, 85°C, recombinant enzyme

707349

4.2.2.13

0.1

-

pH 5.0, 35°C

650299

5.4.99.15

5

-

pH 5.5, 60°C

721858, 722996

5.4.99.15

5.85

-

mutant Y409F, pH 5.0, 60°C

680274

5.4.99.15

5.94

-

wild-type, pH 5.0, 60°C

680274, 680309

5.4.99.15

6.34

-

mutant F405Y, pH 5.0, 60°C

680274, 680309

5.4.99.15

6.6

-

mutant F405M, pH 5.0, 60°C

680309

5.4.99.15

6.6

-

pH 5, 60°C, wild-type enzyme

724886

5.4.99.15

6.6

-

pH 5.0, 60°C, wild-type enzyme

724886

5.4.99.15

7.1

-

-

3488

5.4.99.15

7.9

-

mutant F405W, pH 5.0, 60°C

680309

5.4.99.15

8.7

-

-

3486

5.4.99.15

9.25

-

mutant F405S, pH 5.0, 60°C

680309

5.4.99.15

9.74

-

pH 5.0, 60°C, mutant enzyme P402Q

724886

5.4.99.15

10.1

-

pH 5.0, 60°C, mutant enzyme A406S

724886

5.4.99.15

12.6

-

pH 5.0, 60°C, mutant enzyme V426T

724886

5.4.99.15

43.2

-

pH 5, 60°C, mutant enzyme D411A

724886

5.4.99.15

43.2

-

pH 5.0, 60°C, mutant enzyme D411A

724886

5.4.99.15

43.5

-

pH 5, 60°C, mutant enzyme R614A

724886

5.4.99.15

43.5

-

pH 5.0, 60°C, mutant enzyme R614A

724886

5.4.99.15

122

-

pH 5, 60°C, mutant enzyme D610A

724886

5.4.99.15

122

-

pH 5.0, 60°C, mutant enzyme D610A

724886

5.4.99.15

20 entries

K_i Value (1 result)

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Show KI Value (1 entry)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.2.1.3

0.92

-

pH 5.0, 40°C

728944

References & Links

Literature References (201)

top print hide

Show Reference (201 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

3486

8611744

Purification and properties of a novel enzyme, maltooligosyl trehalose synthase, from Arthrobacter sp. Q36

1995

Nakada, T.; Maruta, K.; Tsusaki, K.; Kubota, M.; Chaen, H.; Sugimoto, T.; Kurimoto, M.; Tsujisaka, Y.

Biosci. Biotechnol. Biochem.

59

2210-2214

3487

8901122

Purification and characterization of new trehalose-producing enzymes isolated from the hyperthermophilic archae, Sulfolobus sulfataricus KM1

1996

Kato, M.; Miura, Y.; Kettoku, M.; Shindo, K.; Iwamatsu, A.; Kobayashi, M.

Biosci. Biotechnol. Biochem.

60

546-550

3488

9063973

Purification and characterization of thermostable maltooligosyl trehalose synthase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius

1996

Nakada, T.; Ikegami, S.; Chaen, H.; Kubota, M.; Fukuda, S.; Sugimoto, T.; Kurimoto, M.; Tsujisaka, Y.

Biosci. Biotechnol. Biochem.

60

263-266

136184

-

Effective purification of glucoamylase in Koji, a solid culture of Aspergillus oryzae on steamed rice, by affinity chromatography using an immobilized acarbose (BAY g-5421)

1988

Ono, K.; Shigeta, S.; Oka, S.

Agric. Biol. Chem.

52

1707-1714

136187

3124820

Purification and properties of an extracellular glucoamylase from a diastatic strain of Saccharomyces cerevisiae

1988

Kleinman, M.J.; Wilkinson, A.E.; Wright, I.P.; Evans, I.H.; Bevan, E.A.

Biochem. J.

249

163-170

136189

3106037

Purification and characterization of extracellular alpha-amylase and glucoamylase from the yeast Candida antarctica CBS 6678

1987

De Mot, R.; Verachtert, H.

Eur. J. Biochem.

164

643-654

136194

-

Kinetic and structural properties of the three forms of glucoamylase of Rhizopus delemar

1985

Abe, J.I.; Nagano, H.; Hizukuri, S.

J. Appl. Biochem.

7

235-247

136196

-

Purification and substrate specificity of glucoamylase of Paecilomyces varioti AHU 9417

1985

Takeda, Y.; Matsui, H.; Tanida, M.; Takao, S.; Chiba, S.

Agric. Biol. Chem.

49

1633-1641

136199

6434506

Fungal glucoamylases

1983

Manjunath, P.; Shenoy, B.C.; Raghavendra Roa, M.R.

J. Appl. Biochem.

5

235-260

136223

9802217

Purification and properties of the raw-starch-digesting glucoamylases from Corticium rolfsii

1998

Nagasaka, Y.; Kurosawa, K.; Yokota, A.; Tomita, F.

Appl. Microbiol. Biotechnol.

50

323-330

136228

9521694

Enzymatic properties of the cysteinesulfinic acid derivative of the catalytic-base mutant Glu400->Cys of glucoamylase from Aspergillus awamori

1998

Fierobe, H.P.; Clarke, A.J.; Tull, D.; Svensson, B.

Biochemistry

37

3753-3759

136231

8679632

Mutational modulation of substrate bond-type specificity and thermostability of glucoamylase from Aspergillus awamori by replacement with short homologue active site sequences and thiol/disulfide engineering

1996

Fierobe, H.P.

Biochemistry

35

8696-8704

136240

9056481

Overexpression and characterization of Aspergillus awamori wild-type and mutant glucoamylase secreted by the methylotrophic yeast Pichia pastoris: comparison with wild-type recombinant glucoamylase produced using Saccharomyces cerevisiae and Aspergillus niger as hosts

1997

Fierobe, H.P.; Mirgorodskaya, E.; Frandsen, T.P.; Roepstorff, P.; Svensson, B.

Protein Expr. Purif.

9

159-170

136241

7716159

Protein engineering of the relative specificity of glucoamylase from Aspergillus awamori based on sequence similarities between starch degrading enzymes

1994

Sierks, M.R.; Svennson, B.

Protein Eng.

7

1479-1484

136242

1777117

Authenticity and reconstitution of immobilized enzymes: characterization and denaturation/renaturation of glucoamylase II

1991

Gottschalk, N.; Jaenicke, R.

Biotechnol. Appl. Biochem.

14

324-335

136427

-

Purification and properties of a thermostable pullulanase from Clostridium thermohydrosulfurogenes EM1 which hydrolyses both alpha-1,6 and alpha-1,4-glycosidic linkages

1990

Spreinat, A.; Antranikian, G.

Appl. Microbiol. Biotechnol.

33

511-518

136429

1444355

Purification and general biochemical properties of thermostable pullulanase from Bacillus stearothermophilus G-82

1992

Kambourova, M.S.; Emanuilova, E.I.

Appl. Biochem. Biotechnol.

33

193-203

136432

7532585

Substrate specificity and detailed characterization of a bifunctional amylase-pullulanase enzyme from Bacillus circulans F-2 having two different active sites on one polypeptide

1995

Kim, C.H.; Kim, Y.S.

Eur. J. Biochem.

227

687-693

136516

2113033

Some properties of monkey intestinal sucrase

1990

Kapadia, H.A.; Sivakami, S.

Indian J. Biochem. Biophys.

27

93-97

136609

-

Purification and some properties of cyclodextrinase from Bacillus coagulans

1983

Kitahata, S.; Taniguchi, M.; Beltran, S.D.; Sugimoto, T.; Okada, S.

Agric. Biol. Chem.

47

1441-1447

136611

5649518

Pattern of action of the amylase and the cyclodextrinase of Bacillus macerans

1968

DePinto, J.A.; Campbell, L.L.

Arch. Biochem. Biophys.

125

253-258

136613

-

Hydrolytic action on various maltosides by an enzyme from Bacillus coagulans

1985

Kitahata, S.; Okada, S.

Carbohydr. Res.

137

217-225

136615

-

Purification and properties of cyclomaltodextrinase from alkalophilic Bacillus sp.

1991

Yoshida, A.; Iwasaki, Y.; Akiba, T.; Horikoshi, K.

J. Ferment. Bioeng.

71

226-229

136617

-

Reclassification of a thermostable alpha-glucosidase from Bacillus subtilis H-17 as a cyclomaltodextrinase

1992

Bradley, M.K.; Lindsay, J.A.

Enzyme Microb. Technol.

14

194-196

136618

1644767

Structure of the gene encoding cyclomaltodextrinase from Clostridium thermohydrosulfuricum 39E and characterization of the enzyme purified from Escherichia coli

1992

Podkovyrov, S.M.; Zeikus, J.G.

J. Bacteriol.

8

5400-5405

136619

-

Purification and characterization of a cyclodextrin-degrading enzyme from Flavobacterium sp.

1993

Bender, H.

Appl. Microbiol. Biotechnol.

39

714-719

136620

-

Purification and properties of the cyclodextrinase of Bacillus sphaericus ATCC 7055

1994

Galvin, N.M.; Kelly, C.T.; Fogarty, W.M.

Appl. Microbiol. Biotechnol.

42

46-50

136738

16535108

Purification and characterization of a maltotetraose-forming alkaline alpha-amylase from an alkalophilic Bacillus strain, GM8901

1995

Kim, T.U.; Gu, B.G.; Jeong, J.Y.; Byun, S.M.; Shin, Y.C.

Appl. Environ. Microbiol.

61

3105-3112

136800

-

Debranching enzymes of potato tubers (Solanum tuberosum L.). I. Purification and some properties of potato isoamylase

1983

Ishizaki, Y.; Taniguchi, H.; Maruyama, Y.; Nakamura, M.

Agric. Biol. Chem.

47

771-779

171378

-

Rabbit muscle amylo-1,6-glucosidase: properties and evidence of heterogeneity

1968

Taylor, P.M.; Whelan, W.J.

Control of Glycogen Metabolism, Proc. FEBS 4th Meeting, Oslo, 1967 (Whelan, W. J. , ed. )

-

101-114

171381

7766615

Effects of oligosaccharide binding on glycogen debranching enzyme activity and conformation

1995

Liu, W.; Madsen, N.B.; Fan, B.; Zucker, K.A.; Glew, R.H.; Fry, D.E.

Biochemistry

34

7056-7061

171733

-

Formation and hydrolysis of maltohexaose by an extracellular exo-maltohexaohydrolase

1983

Monma, M.; Nakakuki, T.; Kainuma, K.

Agric. Biol. Chem.

47

1769-1774

171735

18548722

Immobilization of the exo-maltohexaohydrolase by the irradiation method

1983

Nakakuki, T.; Hayashi, T.; Monma, M.; Kawashima, K.; Kainuma, K.

Biotechnol. Bioeng.

25

1095-1107

171736

-

Production and purification of new maltohexaose-forming amylases from alkalophilic Bacillus sp. H-167

1988

Hayashi, T.; Akiba, T.; Horikoshi, K.

Agric. Biol. Chem.

52

443-448

208638

8690718

Construction of a plasmid used for the expression of a sevenfold-mutant barley beta-amylase with increased thermostability in Escherichia coli and properties of the sevenfold-mutant beta-amylase

1995

Yoshigi, N.; Okada, Y.; Maeba, H.; Sahara, H.; Tamaki, T.

J. Biochem.

118

562-567

208642

8987540

Cloning, sequencing, and expression of a beta-amylase gene from Bacillus cereus var. mycoides and characterization of its products

1996

Yamaguchi, T.; Matsumoto, Y.; Shirakawa, M.; Kibe, M.; Hibino, T.; Kozaki, S.; Takasaki, Y.; Nitta, Y.

Biosci. Biotechnol. Biochem.

60

1255-1259

208643

7765034

Expression in Escherichia coli of cDNA encoding barley beta-amylase and properties of recombinant beta-amylase

1994

Yoshigi, N.; Okada, Y.; Sahara, H.; Koshino, S.

Biosci. Biotechnol. Biochem.

58

1080-1086

393260

2505756

Neutral maltase/glucoamylase from rabbit renal cortex

1989

Pereira, B.; Sivakami, S.

Biochem. J.

261

43-47

393261

-

Low molecular-activity alpha-glucosidase from ungerminated rice seed

1988

Matsui, H.; Ito, H.; Chiba, S.

Agric. Biol. Chem.

52

1859-1860

393282

-

Purification and substrate specificity of sweet corn alpha-glucosidase

1981

Matsui, H.; Yazawa, I.; Chiba, S.

Agric. Biol. Chem.

45

887-894

393319

6767500

Purification by affinity chromatography and characterization of a neutral alpha-glucosidase from horse kidney

1980

Giudicelli, J.; Emiliozzi, R.; Vannier, C.; de Burlet, G.; Sudaka, P.

Biochim. Biophys. Acta

612

85-96

393325

9285074

Purification and biochemical characterisation of human placental acid alpha-glucosidase

1997

Chadalavada, D.M.; Sivakami, S.

Biochem. Mol. Biol. Int.

42

1051-1061

393334

-

Characterization of high pI alpha-glucosidase from germinated barley seeds: substrate specificity subsite affinities and active-site residues

1995

Im, H.; Henson, C.A.

Carbohydr. Res.

277

145-159

393337

-

Purification and properties of alpha-glucosidase from suspension-cultured sugar-beet cells

1991

Yamasaki, Y.; Konno, H.

Phytochemistry

30

2861-2863

393340

-

Substrate specificity and subsite affinities of crystalline alpha-glucosidase from Aspergillus niger

1991

Kita, A.; Matsui, H.; Somoto, A.; Kimura, A.; Takata, M.; Chiba, S.

Agric. Biol. Chem.

55

2327-2335

393341

-

An alpha-glucosidase from perimicrovillar membranes of Dysdercus peruvianus (hemiptera: pyrrhocoridae) midgut cells. Purification and properties

1995

Silva, C.P.; Terra, W.R.

Insect Biochem. Mol. Biol.

25

487-494

393348

2204617

Allosteric properties, substrate specificity and subsite affinities of honeybee alpha-glucosidase I

1990

Kimura, A.; Takewaki, S.; Matsui, H.; Kubota, M.; Chiba, S.

J. Biochem.

107

762-768

393350

10229946

Properties of maltose-inducible alpha-glucosidase MalL (sucrase-isomaltase-maltase) in Bacillus subtilis: evidence for its contribution to maltodextrin utilization

1999

Schoenert, S.; Buder, T.; Dahl, M.K.

Res. Microbiol.

150

167-177

393353

1708385

Characterization of a neopullulanase and an alpha-glucosidase from Bacteroides thetaiotaomicron 95-1

1991

Smith, K.A.; Salyers, A.A.

J. Bacteriol.

173

2962-2968

393356

-

Production and properties of alpha-glucosidase from the thermotolerant bacterium Thermomonospora curvata

1997

Janda, L.; Pavelka, T.; Tichy, P.; Spizek, J.; Petricek, M.

J. Appl. Microbiol.

83

470-476

393365

27320995

Purification and Properties of Amylases Extracellularly Produced by an Imperfect Fungus, Fusidium sp. BX-1 in a Glycerol Medium.

1992

Ohno, N.; Ijuin, T.; Song, S.; Uchiyama, S.; Shinoyama, H.; Ando, A.; Fujii, T.

Biosci. Biotechnol. Biochem.

56

465-471

393367

16667384

Characterization of alpha-amylase from shoots and cotyledons of pea (Pisum sativum L.) seedlings

1990

Beers, E.P.; Duke, S.H.

Plant Physiol.

92

1154-1163

393379

16347662

Production and characterization of raw-potato-starch-digesting alpha-amylase from Bacillus subtilis 65

1988

Hayashida, S.; Teramoto, Y.; Inoue, T.

Appl. Environ. Microbiol.

54

1516-1522

393426

237562

A Pseudomonas intracellular amylase with high activity on maltodextrins and cyclodextrins

1975

Kato, K.; Sugimoto, T.; Amemura, A.; Harada, T.

Biochim. Biophys. Acta

391

96-108

393429

8226989

The purification and characterization of an extremely thermostable alpha-amylase from the hyperthermophilic archaebacterium Pyrococcus furiosus

1993

Laderman, K.A.; Davis, B.R.; Krutzsch, H.C.; Lewis, M.S.; Griko, Y.V.; Privalov, P.L.; Anfinsen, C.B.

J. Biol. Chem.

268

24394-24401

393431

9726872

Enzymatic properties of a novel liquefying alpha-amylase from an alkaliphilic Bacillus isolate and entire nucleotide and amino acid sequences

1998

Igarashi, K.; Hatada, Y.; Hagihara, H.; Saeki, K.; Takaiwa, M.; Uemura, T.; Ara, K.; Ozaki, K.; Kawai, S.; Kobayashi, T.; Ito, S.

Appl. Environ. Microbiol.

64

3282-3289

393450

27396998

Three Different Types of ?-Amylases from Aspergillus awamori KT-11: Their Purifications, Properties, and Specificities.

1998

Anindyawati, T.; Melliawati, R.; Ito, K.; Iizuka, M.; Minamiura, N.

Biosci. Biotechnol. Biochem.

62

1351-1357

393462

-

Ostrich, pancreatic alpha-amylase: kinetic properties, amino terminal sequence and subsite structure

1994

Oosthuizen, V.; Naude, R.J.; Oelofsen, W.; Muramoto, K.; Kamiya, H.

Int. J. Biochem.

26

1313-1321

487512

12731863

The structure and specificity of Escherichia coli maltose acetyltransferase give new insight into the LacA family of acyltransferases

2003

Lo Leggio, L.; Dal Degan, F.; Poulsen, P.; Moeller Andersen, S.; Larsen, S.

Biochemistry

42

5225-5235

488239

12945

1,4-alpha-Glucan phosphorylase from Klebsiella pneumoniae purification, subunit structure and amino acid composition

1976

Linder, D.; Kurz, G.; Bender, H.; Wallenfels, K.

Eur. J. Biochem.

70

291-303

488254

-

Yeast glycogen phosphorylase: kinetic properties compared with muscle and potato enzymes

1988

Tanabe, S.; Kobayashi, M.; Matsuda, K.

Agric. Biol. Chem.

52

757-764

488256

-

Characterization of Chlorella phosphorylase: the glucan specificity and effect of temperature

1983

Nakamura, Y.; Imamura, M.

Phytochemistry

22

2395-2399

488261

-

Purification and some properties of two phosphorylases from Typha latifolia pollen

1988

Iwata, T.; Funagama, T.; Hara, A.

Agric. Biol. Chem.

52

407-412

488262

16661543

Characterization of the spinach leaf phosphorylases

1980

Preiss, J.; Okita, T.W.; Greenberg, E.

Plant Physiol.

66

864-869

488264

4730475

Sweet corn phosphorylase: purification and properties

1973

Lee, E.Y.C.; Braun, J.J.

Arch. Biochem. Biophys.

156

276-286

488265

16665923

Purification and properties of mesophyll and bundle sheath cell alpha-glucan phosphorylases from Zea mays L.

1988

Mateyka, C.; Schnarrenberger, C.

Plant Physiol.

86

417-422

488294

8706700

Purification and characterization of an alpha-glucan phosphorylase from the thermophilic bacterium Thermus thermophilus

1996

Boeck, B.; Schinzel, R.

Eur. J. Biochem.

239

150-155

488295

9307027

alpha-1,4-D-Glucan phosphorylase of gram-positive Corynebacterium callunae: isolation, biochemical properties and molecular shape of the enzyme from solution X-ray scattering

1997

Weinhausel, A.; Griessler, R.; Krebs, A.; Zipper, P.; Haltrich, D.; Kulbe, K.D.; Nidetzky, B.

Biochem. J.

326

773-783

488297

-

Purification and characterization of alpha-glucan phosphorylase from Bacillus stearothermophilus

1998

Takata, H.; Takaha, T.; Okada, S.; Takagi, M.; Imanaka, T.

J. Ferment. Bioeng.

85

156-161

488304

11361132

Purification and characterization of the maize amyloplast stromal 112-kDa starch phosphorylase

2001

Mu, H.H.; Yu, Y.; Wasserman, B.P.; Carman, G.M.

Arch. Biochem. Biophys.

388

155-164

488405

-

UDPG-glycogen transglucosylase

1962

Leloir, L.F.; Cardini, C.E.

The Enzymes, 2nd Ed. (Boyer, P. D. , Lardy, H. , Myrbäck, K. , eds. )

6

317-326

488677

-

Trihalo-trideoxy galactosucrose compounds

1985

Rathbone, E.B.; Hacking, A.J.; Cheetham, P.S.J.

UK Patent Application

GB21

45080 A

488834

-

Purification and properties of cyclomaltodextrin glucanotransferase from an alkalophilic Bacillus

1988

Maekelae, M.; Mattsson, P.; Schinina, M.E.; Korpela, T.

Biotechnol. Appl. Biochem.

10

414-427

488839

-

Purification and properties of Bacillus coagulans cyclomaltodextrin glucanotransferase

1991

Akimaru, K.; Yagi, T.; Yamamoto, S.

J. Ferment. Bioeng.

71

322-328

488862

11879012

Modulation of cyclizing activity and thermostability of cyclodextrin glucanotransferase and its application as an antistaling enzyme

2002

Lee, S.H.; Kim, Y.W.; Lee, S.; Auh, J.H.; Yoo, S.S.; Kim, T.J.; Kim, J.W.; Kim, S.T.; Rho, H.J.; Choi, J.H.; Kim, Y.B.; Park, K.H.

J. Agric. Food Chem.

50

1411-1415

488876

-

Purification and some properties of dextrin dextranase from Acetobacter capsulatus ATCC 11894

1992

Yamamoto, K.; Yoshikawa, K.; Kitahata, S.; Okada, S.

Biosci. Biotechnol. Biochem.

56

169-173

488882

-

Functional characteristics of a bacterial dextrin dextranase from Acetobacter capsulatum ATCC 11894

2001

Suzuki, M.; Unno, T.; Okada, G.

J. Appl. Glycosci.

48

143-151

488926

-

Granule-bound starch synthase I in isolated starch granules elongates malto-oligosaccharides processively

1999

Denyer, K.; Waite, D.; Motawia, S.; Moller, B.L.; Smith, A.M.

Biochem. J.

340

183-191

488995

4972097

The isolation and mode of action of a bacterial glucanosyltransferase

1968

Pazur, J.H.; Okada, S.

J. Biol. Chem.

243

4732-4738

488997

791642

The action pattern of amylomaltase from Escherichia coli

1976

Palmer, T.N.; Ryman, B.; Whelan, W.J.

Eur. J. Biochem.

69

105-115

488998

758954

Starch metabolism in Pseudomonas stutzeri. II. Purification and properties of a dextrin glycosyl-transferase (D-enzyme) and amylomaltase

1979

Schmidt, J.; John, M.

Biochim. Biophys. Acta

566

100-114

489000

16665877

Characterization of D-enzyme (4-alpha-glucanotransferase) in Arabidopsis leaf

1988

Lin, T.P.; Preiss, J.

Plant Physiol.

86

260-265

489001

16666985

Characterization of pea chloroplast D-enzyme (4-alpha-D-glucanotransferase)

1989

Kakefuda, G.; Duke, S.H.

Plant Physiol.

91

136-143

489002

-

Purification and some properties of amylomaltase from Escherichia coli IFO 3806

1989

Kitahata, S.; Murakami, H.; Okada, S.

Agric. Biol. Chem.

53

2653-2659

489004

-

Analysis of the characteristic action of D-enzyme from sweet potato in terms of subsite theory

1991

Toshihiko, S.; Shinji, S.; Shigeo, F.; Tomonori, N.

Carbohydr. Res.

212

201-212

489005

1628664

Purification and characterization of a novel thermostable 4-alpha-glucanotransferase of Thermotoga maritima cloned in Escherichia coli

1992

Liebl, W.; Feil, R.; Gabelsberger, J.; Kellermann, J.; Schleifer, K.H.

Eur. J. Biochem.

207

81-88

489007

7678257

Disproportionating enzyme (4-alpha-glucanotransferase; EC 2.4.1.25) of potato. Purification, molecular cloning, and potential role in starch metabolism

1993

Takaha, T.; Yanase, M.; Okada, S.; Smith, S.M.

J. Biol. Chem.

268

1391-1396

489010

9310375

4-alpha-glucanotransferase from the hyperthermophilic archaeon Thermococcus litoralis. Enzyme purification and characterization, and gene cloning, sequencing and expression in Escherichia coli

1997

Jeon, B.S.; Taguchi, H.; Sakai, H.; Ohshima, T.; Wakagi, T.; Matsuzawa, H.

Eur. J. Biochem.

248

171-178

489011

-

Cloning and expression of the 4-alpha-glucanotransferase gene from the hyperthermophilic archaeon Pyrococcus sp. KOD1, and characterization of the enzyme

1997

Tachibana, Y.; Fujiwara, S.; Takagi, M.; Imanaka, T.

J. Ferment. Bioeng.

83

540-548

489012

-

Gene and properties of thermostable 4-alpha-glucanotransferase of Thermotoga neapolitana

1999

Berezina, O.V.; Zverlov, V.V.; Lunina, N.A.; Chekanovskaya, L.A.; Dubinia, E.N.; Liebl, W.; Velikodvorskaya, G.A.

Mol. Biol.

33

801-806

489014

10444083

Biochemical characterization of the Chlamydomonas reinhardtii alpha-1,4 glucanotransferase supports a direct function in amylopectin biosynthesis

1999

Colleoni, C.; Dauvillee, D.; Mouille, G.; Morell, M.; Samuel, M.; Slomiany, M.C.; Lienard, L.; Wattebled, F.; d'Hulst, C.; Ball, S.

Plant Physiol.

120

1005-1014

489015

10471815

High level expression of Thermococcus litoralis 4-alpha-glucanotransferase in a soluble form in Escherichia coli with a novel expression system involving minor arginine tRNAs and GroELS

1999

Imamura, H.; Jeon, B.; Wakagi, T.; Matsuzawa, H.

FEBS Lett.

457

393-396

489016

10049841

Thermus aquaticus ATCC 33923 amylomaltase gene cloning and expression and enzyme characterization: production of cycloamylose

1999

Terada, Y.; Fujii, K.; Takaha, T.; Okada, S.

Appl. Environ. Microbiol.

65

910-915

489019

10677288

Crystal structure of amylomaltase from Thermus aquaticus, a glycosyltransferase catalyzing the production of large cyclic glucans

2000

Przylas, I.; Tomoo, K.; Terada, Y.; Takaha, T.; Fujii, K.; Saenger, W.; Strater, N.

J. Mol. Biol.

296

873-886

489020

-

Amylomaltase from the hyperthermophilic bacterium Thermus thermophilus: Enzyme characteristics and application in the starch industry

2000

Van der Maarel, M.J.E.C.; Euverink, G.J.W.; Binnema, D.J.; Bos, H.T.P.; Bergsma, J.

Meded. -Fac. Landbouwkd. Toegepaste Biol. Wet.

65

231-234

489022

12618437

Crystal structures of 4-alpha-glucanotransferase from Thermococcus litoralis and its complex with an inhibitor

2003

Imamura, H.; Fushinobu, S.; Yamamoto, M.; Kumasaka, T.; Jeon, B.S.; Wakagi, T.; Matsuzawa, H.

J. Biol. Chem.

278

19378-19386

489140

-

Studies on a recombinant amylosucrase

1995

Remaud-Simeon, M.; Albaret, F.; Canard, B.; Varlet, I.; Colonna, P.; Willemot, R.M.; Monsan, P.

Prog. Biotechnol.

10

313-320

646647

-

Studies on enzymic production of oligosaccharides. Part VI. Maltotriose-producing amylase from Microbacterium imperiale

1991

Takasaki, Y.; Kitajima, M.; Tsuruta, T.; Nonoguchi, M.; Hayashi, S.; Imada, K.

Agric. Biol. Chem.

55

687-692

646648

1592801

Haloalkaliphilic maltotriose-forming alpha-amylase from the archaebacterium Natronococcus sp. strain Ah-36

1992

Kobayashi, T.; Kanai, H.; Hayashi, T.; Akiba, T.; Akaboshi, R.; Horikoshi, K.

J. Bacteriol.

174

3439-3444

646816

11916682

Bacillus stearothermophilus neopullulanase selective hydrolysis of amylose to maltose in the presence of amylopectin

2002

Kamasaka, H.; Sugimoto, K.; Takata, H.; Nishimura, T.; Kuriki, T.

Appl. Environ. Microbiol.

68

1658-1664

649108

-

Crystallization and improvement of crystal quality for X-ray diffraction of maltooligosyl trehalose synthase by reductive methylation of lysine residues

1999

Kobayashi, M.; Kubota, M.; Matsuura, Y.

Acta Crystallogr. Sect. D

55

931-933

650299

10564758

Characterization of exo-(1,4)-alpha glucan lyase from red alga Gracilaria chorda. Activation, inactivation and the kinetic properties of the enzyme

1999

Yoshinaga, K.; Fujisue, M.; Abe, J.; Hanashiro, I.; Takeda, Y.; Muroya, K.; Hizukuri, S.

Biochim. Biophys. Acta

1472

447-454

651359

11164309

Characterization of the maltooligosyl trehalose synthase from the thermophilic archaeon Sulfolobus acidocaldarius

2001

Gueguen, Y.; Rolland, J.L.; Schroeck, S.; Flament, D.; Defretin, S.; Saniez, M.H.; Dietrich, J.

FEMS Microbiol. Lett.

194

201-206

654259

11872475

Novel alpha-glucosidase from Aspergillus nidulans with strong transglycosylation activity

2002

Kato, N.; Suyama, S.; Shirokane, M.; Kato, M.; Kobayashi, T.; Tsukagoshi, N.

Appl. Environ. Microbiol.

68

1250-1256

654643

11914097

Mechanistic analyses of catalysis in human pancreatic alpha-amylase: detailed kinetic and structural studies of mutants of three conserved carboxylic acids

2002

Rydberg, E.H.; Li, C.; Maurus, R.; Overall, C.M.; Brayer, G.D.; Withers, S.G.

Biochemistry

41

4492-4502

654708

12741813

Crystal structure of a catalytic site mutant of beta-amylase from Bacillus cereus var. mycoides cocrystallized with maltopentaose

2003

Miyake, H.; Kurisu, G.; Kusunoki, M.; Nishimura, S.; Kitamura, S.; Nitta, Y.

Biochemistry

42

5574-5581

654806

11150611

Glucoamylase: structure/function relationships, and protein engineering

2000

Sauer, J.; Sigurskjold, B.W.; Christensen, U.; Frandsen, T.P.; Mirgorodskaya, E.; Harrison, M.; Roepstorff, P.; Svensson, B.

Biochim. Biophys. Acta

1543

275-293

654808

11341943

Comparison of sucrase-free isomaltase with sucrase-isomaltase purified from the house musk shrew Suncus murinus

2001

Takesue, Y.; Yokota, K.; Oda, S.; Takesue, S.

Biochim. Biophys. Acta

1544

341-349

655000

11515546

Purification and substrate specificity of honeybee, Apis mellifera L., alpha-glucosidase III

2001

Nishimoto, M.; Kubota, M.; Tsuji, M.; Mori, H.; Kimura, A.; Matsui, H.; Chiba, S.

Biosci. Biotechnol. Biochem.

65

1610-1616

655023

12506981

Purification and characterization of a novel fungal alpha-glucosidase from Mortierella alliacea with high starch-hydrolytic activity

2002

Tanaka, Y.; Aki, T.; Hidaka, Y.; Furuya, Y.; Kawamoto, S.; Shigeta, S.; Ono, K.; Suzuki, O.

Biosci. Biotechnol. Biochem.

66

2415-2423

655050

12619670

Purification and characterization of a new type of alpha-glucosidase from Paecilomyces lilacinus that has transglucosylation activity to produce alpha-1,3- and alpha-1,2-linked oligosaccharides

2003

Kobayashi, I.; Tokuda, M.; Hashimoto, H.; Konda, T.; Nakano, H.; Kitahata, S.

Biosci. Biotechnol. Biochem.

67

29-35

655083

-

Production and characterization of extracellular alpha-amylases from the thermophilic fungus Thermomyces lanuginosus (wild and mutant strains)

2000

Petrova, S.D.; Ilieva, S.Z.; Bakalova, N.G.; Atev, A.P.; Bhat, M.K.; Kolev, D.N.

Biotechnol. Lett.

22

1619-1624

655912

11926997

Catalytic mechanism of beta-amylase from Bacillus cereus var. mycoides: chemical rescue of hydrolytic activity for a catalytic site mutant (Glu367-->Ala) by azide

2002

Miyake, H.; Otsuka, C.; Nishimura, S.; Nitta, Y.

J. Biochem.

131

587-591

655918

12761294

Crystal structures of beta-amylase from Bacillus cereus var. mycoides in complexes with substrate analogs and affinity-labeling reagents

2003

Oyama, T.; Miyake, H.; Kusunoki, M.; Nitta, Y.

J. Biochem.

133

467-474

655927

15113834

Two additional carbohydrate-binding sites of beta-amylase from Bacillus cereus var. mycoides are involved in hydrolysis and raw starch-binding

2004

Ye, Z.; Miyake, H.; Tatsumi, M.; Nishimura, S.; Nitta, Y.

J. Biochem.

135

355-363

656390

11001140

Purification and specificity of two alpha-glucosidase isoforms of the parasitic protist Trichomonas vaginalis

2000

Ter Kuile, B.H.; Hrdy, I.; Sanchez, L.B.; Muller, M.

J. Eukaryot. Microbiol.

47

440-442

656677

12081555

Characterization of a salt-tolerant extracellular alpha-amylase from Bacillus dipsosauri

2002

Deutch, C.E.

Lett. Appl. Microbiol.

35

78-84

656678

12641711

Production and partial characterization of a beta-amylase by Xanthophyllomyces dendrorhous

2003

Diaz, A.; Sieiro, C.; Villa, T.G.

Lett. Appl. Microbiol.

36

203-207

656703

11210505

alpha-Glucosidase from Pyrococcus furiosus

2001

Chang, S.T.; Parker, K.N.; Bauer, M.W.; Kelly, R.M.

Methods Enzymol.

330

260-269

656955

14561508

beta-Amylase in germinating millet seeds

2003

Yamasaki, Y.

Phytochemistry

64

935-939

657123

11469591

Copy-DNA cloning and characterisation of a potato alpha-glucosidase: expression in Escherichia coli and effects of down-regulation in transgenic potato

2001

Taylor, M.A.; Ross, H.A.; McRae, D.; Wright, F.; Viola, R.; Davies, H.V.

Planta

213

258-264

657863

15535798

Catalytic mechanism of alpha-retaining glucosyl transfer by Corynebacterium callunae starch phosphorylase: the role of histidine-334 examined through kinetic characterization of site-directed mutants

2005

Schwarz, A.; Pierfederici, F.M.; Nidetzky, B.

Biochem. J.

387

437-445

658355

-

Purification and characterization of a cytosolic starch phosphorylase from etiolated rice seedlings

2004

Hsu, J.H.; Yang, C.C.; Su, J.C.; Lee, P.D.

Bot. Bull. Acad. Sin.

45

187-196

659735

-

Characterization of a hyperthermostable glycogen phosphorylase from Aquifex aeolicus expressed in Escherichia coli

2003

Bhuiyan, S.H.; Rus'd, A.A.; Kitaoka, M.; Hayashi, K.

J. Mol. Catal. B

22

173-180

660766

16151092

Amylomaltase of Pyrobaculum aerophilum IM2 produces thermoreversible starch gels

2005

Kaper, T.; Talik, B.; Ettema, T.J.; Bos, H.; van der Maarel, M.J.; Dijkhuizen, L.

Appl. Environ. Microbiol.

71

5098-5106

661611

-

Purification and characterization of the hyper-glycosylated extracellular alpha-glucosidase from Schizosaccharomyces pombe

2005

Okuyama, M.; Tanimoto, Y.; Ito, T.; Anzai, A.; Mori, H.; Kimura, A.; Matsui, H.; Chiba, S.

Enzyme Microb. Technol.

37

472-480

662665

-

A cycloamylose-forming hyperthermostable 4-alpha-glucanotransferase of Aquifex aeolicus expressed in Escherichia coli

2003

Bhuiyan, S.H.; Kitaoka, M.; Hayashi, K.

J. Mol. Catal. B

22

45-53

663981

16509822

The family 21 carbohydrate-binding module of glucoamylase from Rhizopus oryzae consists of two sites playing distinct roles in ligand binding

2006

Chou, W.I.; Pai, T.W.; Liu, S.H.; Hsiung, B.K.; Chang, M.D.

Biochem. J.

396

469-477

664208

15975859

Mutagenesis of Ala290, which modulates substrate subsite affinity at the catalytic interface of dimeric ThMA

2005

Park, S.; Cha, H.; Kang, H.; Shim, J.; Woo, E.; Kim, J.; Park, K.

Biochim. Biophys. Acta

1751

170-177

664362

14981306

Purification, characterization, and subsite affinities of Thermoactinomyces vulgaris R-47 maltooligosaccharide-metabolizing enzyme homologous to glucoamylases

2004

Ichikawa, K.; Tonozuka, T.; Uotsu-Tomita, R.; Akeboshi, H.; Nishikawa, A.; Sakano, Y.

Biosci. Biotechnol. Biochem.

68

413-420

664779

-

Purification and characterization of cyclodextrinase from Paenibacillus sp. A11

2005

Kaulpiboon, J.; Pongsawasdi, P.

Enzyme Microb. Technol.

36

168-175

664980

15043869

Cloning and expression of Lipomyces starkeyi alpha-amylase in Escherichia coli and determination of some of its properties

2004

Kang, H.K.; Lee, J.H.; Kim, D.; Day, D.F.; Robyt, J.F.; Park, K.H.; Moon, T.W.

FEMS Microbiol. Lett.

233

53-64

665013

-

Purification and characterization of three amylases from viscera of hard clam Meretrix lusoria

2004

Tsao, C.; Hsu, Y.; Chao, L.; Jiang, S.

Fish. Sci.

70

174-182

665437

15469727

Expression of cyclodextrinase gene from Paenibacillus sp. A11 in Escherichia coli and characterization of the purified cyclodextrinase

2004

Kaulpiboon, J.; Pongsawasdi, P.

J. Biochem. Mol. Biol.

37

408-415

666019

15178253

The roles of Glu186 and Glu380 in the catalytic reaction of soybean beta-amylase

2004

Kang, Y.N.; Adachi, M.; Utsumi, S.; Mikami, B.

J. Mol. Biol.

339

1129-1140

666785

-

alpha-Amylase from B. amyloliquefaciens: purification, characterization, raw starch degradation and expression in E. coli

2005

Demirkan, E.S.; Mikami, B.; Adachi, M.; Higasa, T.; Utsumi, S.

Process Biochem.

40

2629-2636

677784

18080814

A thermoactive glucoamylase with biotechnological relevance from the thermoacidophilic euryarchaeon Thermoplasma acidophilum

2008

Dock, C.; Hess, M.; Antranikian, G.

Appl. Microbiol. Biotechnol.

78

105-114

678461

17468058

Molecular cloning and biochemical characterization of the first archaeal maltogenic amylase from the hyperthermophilic archaeon Thermoplasma volcanium GSS1

2007

Kim, J.W.; Kim, Y.H.; Lee, H.S.; Yang, S.J.; Kim, Y.W.; Lee, M.H.; Kim, J.W.; Seo, N.S.; Park, C.S.; Park, K.H.

Biochim. Biophys. Acta

1774

661-669

678787

17151473

Purification and characterization of alpha-glucosidase I from Japanese honeybee (Apis cerana japonica) and molecular cloning of its cDNA

2006

Wongchawalit, J.; Yamamoto, T.; Nakai, H.; Kim, Y.M.; Sato, N.; Nishimoto, M.; Okuyama, M.; Mori, H.; Saji, O.; Chanchao, C.; Wongsiri, S.; Surarit, R.; Svasti, J.; Chiba, S.; Kimura, A.

Biosci. Biotechnol. Biochem.

70

2889-2898

678799

17690465

Purification, biochemical characterization, and gene cloning of a new extracellular thermotolerant and glucose tolerant maltooligosaccharide-forming alpha-amylase from an endophytic ascomycete Fusicoccum sp. BCC4124

2007

Champreda, V.; Kanokratana, P.; Sriprang, R.; Tanapongpipat, S.; Eurwilaichitr, L.

Biosci. Biotechnol. Biochem.

71

2010-2020

678808

17928688

Purification and characterization of heterogeneous glucoamylases from Monascus purpureus

2007

Tachibana, S.; Yasuda, M.

Biosci. Biotechnol. Biochem.

71

2573-2576

678813

18071262

Molecular cloning and characterization of an alpha-amylase from Pichia burtonii 15-1

2007

Kato, S.; Shimizu-Ibuka, A.; Mura, K.; Takeuchi, A.; Tokue, C.; Arai, S.

Biosci. Biotechnol. Biochem.

71

3007-3013

680274

19127729

Mutations on aromatic residues of the active site to alter selectivity of the Sulfolobus solfataricus maltooligosyltrehalose synthase

2006

Fang, T.; Tseng, W.; Chung, Y.; Pan, C.

J. Agric. Food Chem.

54

3585-3590

680283

16968069

Expression, purification, and characterization of the maltooligosyltrehalose trehalohydrolase from the thermophilic archaeon Sulfolobus solfataricus ATCC 35092

2006

Fang, T.Y.; Tseng, W.C.; Guo, M.S.; Shih, T.Y.; Hung, X.G.

J. Agric. Food Chem.

54

7105-7112

680309

17567140

Protein engineering of Sulfolobus solfataricus maltooligosyltrehalose synthase to alter its selectivity

2007

Fang, T.Y.; Tseng, W.C.; Pan, C.H.; Chun, Y.T.; Wang, M.Y.

J. Agric. Food Chem.

55

5588-5594

680469

17015651

Molecular and biochemical characterization of alpha-glucosidase and alpha-mannosidase and their clustered genes from the thermoacidophilic archaeon Picrophilus torridus

2006

Angelov, A.; Putyrski, M.; Liebl, W.

J. Bacteriol.

188

7123-7131

681347

18051363

Molecular cloning and characterization of trehalose biosynthesis genes from hyperthermophilic archaebacterium Metallosphaera hakonesis

2007

Seo, J.S.; An, J.H.; Baik, M.Y.; Park, C.S.; Cheong, J.J.; Moon, T.W.; Park, K.H.; Choi, Y.D.; Kim, C.H.

J. Microbiol. Biotechnol.

17

123-129

685153

17407266

Identification of acceptor substrate binding subsites +2 and +3 in the amylomaltase from Thermus thermophilus HB8

2007

Kaper, T.; Leemhuis, H.; Uitdehaag, J.C.; van der Veen, B.A.; Dijkstra, B.W.; van der Maarel, M.J.; Dijkhuizen, L.

Biochemistry

46

5261-5269

685689

18323642

Purification and characterization of a carbohydrate: acceptor oxidoreductase from Paraconiothyrium sp. that produces lactobionic acid efficiently

2008

Kiryu, T.; Nakano, H.; Kiso, T.; Murakami, H.

Biosci. Biotechnol. Biochem.

72

833-841

686672

17803683

Probing the active site of Corynebacterium callunae starch phosphorylase through the characterization of wild-type and His334-->Gly mutant enzymes

2007

Schwarz, A.; Brecker, L.; Nidetzky, B.

FEBS J.

274

5105-5115

692116

-

Synthesis of novel disaccharides by a newly isolated fructosyl transferase from Bacillus subtilis

1989

Cheetham, P.S.; Hacking, A.J.; Vlitos, M.

Enzyme Microb. Technol.

11

212-219

692727

18563901

Identification of the essential catalytic residues and selectivity-related residues of maltooligosyltrehalose trehalohydrolase from the thermophilic archaeon Sulfolobus solfataricus ATCC 35092

2008

Fang, T.Y.; Tseng, W.C.; Shih, T.Y.; Wang, M.Y.

J. Agric. Food Chem.

56

5628-5633

693604

18467868

Effects of calcium ion concentration on starch hydrolysis of barley alpha-amylase isozymes

2008

Yuk, J.B.; Choi, S.H.; Lee, T.H.; Jang, M.U.; Park, J.M.; Yi, A.R.; Svensson, B.; Kim, T.J.

J. Microbiol. Biotechnol.

18

730-734

693790

18356321

Luminal starch substrate "brake" on maltase-glucoamylase activity is located within the glucoamylase subunit

2008

Quezada-Calvillo, R.; Sim, L.; Ao, Z.; Hamaker, B.R.; Quaroni, A.; Brayer, G.D.; Sterchi, E.E.; Robayo-Torres, C.C.; Rose, D.R.; Nichols, B.L.

J. Nutr.

138

685-692

698519

-

A novel glucanotransferase that produces a cyclomaltopentaose cyclized by an alpha-1,6-linkage

2007

Watanabe, H.; Nishimoto, T.; Chaen, H.; Fukuda, S.

J. Appl. Glycosci.

54

109-118

699548

18586271

Structural insights into the substrate specificity and function of Escherichia coli K12 YgjK, a glucosidase belonging to the glycoside hydrolase family 63

2008

Kurakata, Y.; Uechi, A.; Yoshida, H.; Kamitori, S.; Sakano, Y.; Nishikawa, A.; Tonozuka, T.

J. Mol. Biol.

381

116-128

701883

19834705

Characterization of an exo-acting intracellular alpha-amylase from the hyperthermophilic bacterium Thermotoga neapolitana

2010

Park, K.M.; Jun, S.Y.; Choi, K.H.; Park, K.H.; Park, C.S.; Cha, J.

Appl. Microbiol. Biotechnol.

86

555-566

701969

19054743

Recombinant production and biochemical characterization of a hyperthermostable alpha-glucan/maltodextrin phosphorylase from Pyrococcus furiosus

2008

Mizanur, R.M.; Griffin, A.K.; Pohl, N.L.

Archaea

2

169-176

702452

19682609

"Short-chain" alpha-1,4-glucan phosphorylase having a truncated N-terminal domain: functional expression and characterization of the enzyme from Sulfolobus solfataricus

2009

Mueller, M.; Takemasa, R.; Schwarz, A.; Atomi, H.; Nidetzky, B.

Biochim. Biophys. Acta

1794

1709-1714

703502

-

Purification and characterization of a novel amylopullulanase that converts pullulan to glucose, maltose, and maltotriose and starch to glucose and maltose

2010

Zareian, S.; Khajeh, K.; Ranjbar, B.; Dabirmanesh, B.; Ghollasi, M.; Mollania, N.

Enzyme Microb. Technol.

46

57-63

705085

18388462

Purification and characterization of branching specificity of a novel extracellular amylolytic enzyme from marine hyperthermophilic Rhodothermus marinus

2008

Yoon, S.A.; Ryu, S.I.; Lee, S.B.; Moon, T.W.

J. Microbiol. Biotechnol.

18

457-464

707248

19707756

Characterization of a recombinant amylolytic enzyme of hyperthermophilic archaeon Thermofilum pendens with extremely thermostable maltogenic amylase activity

2010

Li, X.; Li, D.; Yin, Y.; Park, K.H.

Appl. Microbiol. Biotechnol.

85

1821-1830

707265

20155355

Cloning, expression, and characterization of a thermostable glucoamylase from Thermoanaerobacter tengcongensis MB4

2010

Zheng, Y.; Xue, Y.; Zhang, Y.; Zhou, C.; Schwaneberg, U.; Ma, Y.

Appl. Microbiol. Biotechnol.

87

225-233

707349

12127967

A novel amylolytic enzyme from Thermotoga maritima, resembling cyclodextrinase and alpha-glucosidase, that liberates glucose from the reducing end of the substrates

2002

Lee, M.; Kim, Y.-W.; Kim, T.-J.; Park, C.-S.; Kim, J.-W.; Moon, T.-W.; Park, K.-H.

Biochem. Biophys. Res. Commun.

295

818-825

708224

19766731

Purification and partial characterization of a midgut membrane-bound alpha-glucosidase from Quesada gigas (Hemiptera: Cicadidae)

2010

Fonseca, F.V.; Silva, J.R.; Samuels, R.I.; DaMatta, R.A.; Terra, W.R.; Silva, C.P.

Comp. Biochem. Physiol. B

155

20-25

709498

20075617

Recombinant expression and characterization of Thermoanaerobacter tengcongensis thermostable alpha-glucosidase with regioselectivity for high yield isomaltooligosaccharides synthesis

2009

Zhou, C.; Xue, Y.; Zhang, Y.; Zeng, Y.; Ma, Y.

J. Microbiol. Biotechnol.

19

1547-1556

717106

20549574

Catalytic properties of two Rhizopus oryzae 99-880 glucoamylase enzymes without starch binding domains expressed in Pichia pastoris

2010

Mertens, J.A.; Braker, J.D.; Jordan, D.B.

Appl. Biochem. Biotechnol.

162

2197-2213

717984

20799086

Purification and characterization of the alpha-glucosidase produced by thermophilic fungus Thermoascus aurantiacus CBMAI 756

2010

Carvalho, A.F.; Boscolo, M.; da Silva, R.; Ferreira, H.; Gomes, E.

J. Microbiol.

48

452-459

721349

21948833

4,6-alpha-Glucanotransferase, a novel enzyme that structurally and functionally provides an evolutionary link between glycoside hydrolase enzyme families 13 and 70

2011

Kralj, S.; Grijpstra, P.; van Leeuwen, S.S.; Leemhuis, H.; Dobruchowska, J.M.; van der Kaaij, R.M.; Malik, A.; Oetari, A.; Kamerling, J.P.; Dijkhuizen, L.

Appl. Environ. Microbiol.

77

8154-8163

721858

27281155

Reaction mechanism of a new glycosyltrehalose-producing enzyme isolated from the hyperthermophilic archaeum, Sulfolobus solfataricus KM1

1996

Kato, M.; Miura, Y.; Kettoku, M.; Shindo, K.; Iwamatsu, A.; Kobayashi, K.

Biosci. Biotechnol. Biochem.

60

921-924

722938

23314368

Enzymatic properties of a thermostable alpha-glucosidase from acidothermophilic crenarchaeon Sulfolobus tokodaii strain 7

2013

Park, J.E.; Park, S.H.; Woo, J.Y.; Hwang, H.S.; Cha, J.; Lee, H.

J. Microbiol. Biotechnol.

23

56-63

722996

-

Trehalose production with a new enzymatic system from Sulfolobus solfataricus KM1

1999

Kato, M.

J. Mol. Catal. B

6

223-233

724097

23884203

Maltose-forming alpha-amylase from the hyperthermophilic archaeon Pyrococcus sp. ST04

2014

Jung, J.H.; Seo, D.H.; Holden, J.F.; Park, C.S.

Appl. Microbiol. Biotechnol.

98

2121-2131

724886

24564903

Identification of substrate-binding and selectivity-related residues of maltooligosyltrehalose synthase from the thermophilic archaeon Sulfolobus solfataricus ATCC 35092

2014

Tseng, W.C.; Lin, C.R.; Hung, X.G.;, Wei, T.Y.; Chen, Y.C.; Fang, T.Y.

Enzyme Microb. Technol.

56

53-59

724948

15150700

Characterization of the trehalosyl dextrin-forming enzyme from the thermophilic archaeon Sulfolobus solfataricus ATCC 35092

2004

Fang, T.Y.; Hung, X.G.; Shih, T.Y.; Tseng, W.C.

Extremophiles

8

335-343

725283

23396915

Identification and characterization of MalA in the maltose/maltodextrin operon of Sulfolobus acidocaldarius DSM639

2013

Choi, K.H.; Hwang, S.; Cha, J.

J. Bacteriol.

195

1789-1799

727388

24835094

Bioinformatic and biochemical analysis of a novel maltose-forming alpha-amylase of the GH57 family in the hyperthermophilic archaeon Thermococcus sp. CL1

2014

Jeon, E.J.; Jung, J.H.; Seo, D.H.; Jung, D.H.; Holden, J.F.; Park, C.S.

Enzyme Microb. Technol.

60

9-15

728944

24468405

Glucoamylase of Caulobacter crescentus CB15: Cloning and expression in Escherichia coli and functional identification

2014

Sakaguchi, M.; Matsushima, Y.; Nankumo, T.; Seino, J.; Miyakawa, S.; Honda, S.; Sugahara, Y.; Oyama, F.; Kawakita, M.

AMB Express

4

5

729090

25038927

An exceptionally cold-adapted alpha-amylase from a metagenomic library of a cold and alkaline environment

2015

Vester, J.; Glaring, M.; Stougaard, P.

Appl. Microbiol. Biotechnol.

99

717-727

729911

11443082

Identification, cloning, expression, and characterization of the extracellular acarbose-modifying glycosyltransferase, AcbD, from Actinoplanes sp. strain SE50

2001

Hemker, M.; Stratmann, A.; Goeke, K.; Schröder, W.; Lenz, J.; Piepersberg, W.; Pape, H.

J. Bacteriol.

183

4484-4492

731585

24345719

Characterization and mechanism of action of Microbacterium imperiale glucan 1,4-alpha-maltotriohydrolase

2014

Wu, C.; Zhou, X.; Xu, Y.; Li, H.; Tian, Y.; Xu, X.; Jin, Z.

Carbohydr. Res.

384

46-50

731665

-

Gene cloning, expression and enzymatic characterization of a high maltose-producing alpha-amylase from Saccharomonospora viridis

2013

Wang, X.; Li, M.; Li, X.; Huang, J.; Huang, Y.; Du, L.; Huang, R.; Wei, Y.

Chin. J. Appl. Environ. Biol.

19

342-345

735356

23695246

Structure of starch synthase I from barley: insight into regulatory mechanisms of starch synthase activity

2013

Cuesta-Seijo, J.A.; Nielsen, M.M.; Marri, L.; Tanaka, H.; Beeren, S.R.; Palcic, M.M.

Acta Crystallogr. Sect. D

69

1013-1025

735514

26590275

The Exiguobacterium sibiricum 255-15 GtfC enzyme represents a novel glycoside hydrolase 70 subfamily of 4,6-alpha-glucanotransferase enzymes

2016

Gangoiti, J.; Pijning, T.; Dijkhuizen, L.

Appl. Environ. Microbiol.

82

756-766

735534

22361861

4,6-alpha-Glucanotransferase activity occurs more widespread in Lactobacillus strains and constitutes a separate GH70 subfamily

2013

Leemhuis, H.; Dijkman, W.; Dobruchowska, J.; Pijning, T.; Grijpstra, P.; Kralj, S.; Kamerling, J.; Dijkhuizen, L.

Appl. Microbiol. Biotechnol.

97

181-193

735717

26868718

The Gram-negative bacterium Azotobacter chroococcum NCIMB 8003 employs a new glycoside hydrolase family 70 4,6-alpha-glucanotransferase enzyme (GtfD) to synthesize a reuteran like polymer from maltodextrins and starch

2016

Gangoiti, J.; van Leeuwen, S.S.; Vafiadi, C.; Dijkhuizen, L.

Biochim. Biophys. Acta

1860

1224-1236

735805

24801911

Essential role of amino acid position 226 in oligosaccharide elongation by amylosucrase from Neisseria polysaccharea

2014

Cambon, E.; Barbe, S.; Pizzut-Serin, S.; Remaud-Simeon, M.; Andre, I.

Biotechnol. Bioeng.

111

1719-1728

736158

26858729

In vitro biochemical characterization of all barley endosperm starch synthases

2015

Cuesta-Seijo, J.A.; Nielsen, M.M.; Ruzanski, C.; Krucewicz, K.; Beeren, S.R.; Rydhal, M.G.; Yoshimura, Y.; Striebeck, A.; Motawia, M.S.; Willats, W.G.; Palcic, M.M.

Front. Plant Sci.

6

1265

736255

26875536

Mutagenesis for improvement of activity and thermostability of amylomaltase from Corynebacterium glutamicum

2016

Nimpiboon, P.; Kaulpiboon, J.; Krusong, K.; Nakamura, S.; Kidokoro, S.; Pongsawasdi, P.

Int. J. Biol. Macromol.

86

820-828

737088

26367870

The role of cysteine residues in redox regulation and protein stability of Arabidopsis thaliana starch synthase 1

2015

Skryhan, K.; Cuesta-Seijo, J.A.; Nielsen, M.M.; Marri, L.; Mellor, S.B.; Glaring, M.A.; Jensen, P.E.; Palcic, M.M.; Blennow, A.

PLoS ONE

10

e0136997

748424

-

Characterization of the catalytic and kinetic properties of a thermostable Thermoplasma acidophilum alpha-glucosidase and its transglucosylation reaction with arbutin

2011

Seo, S.; Choi, K.; Hwang, S.; Kim, J.; Park, C.; Rho, J.; Cha, J.

J. Mol. Catal. B

72

305-312

749728

25620369

Characterization and gene cloning of a maltotriose-forming exo-amylase from Kitasatospora sp. MK-1785

2015

Kamon, M.; Sumitani, J.; Tani, S.; Kawaguchi, T.; Kamon, M.; Sumitani, J.; Tani, S.; Kawaguchi, T.

Appl. Microbiol. Biotechnol.

99

4743-4753

750105

30122147

Enzymatic characterization of an extracellular glucoamylase from Tricholoma matsutake and its cloning and secretory expression in Pichia pastoris

2018

Onuma, H.; Uchiyama, H.; Hara, K.; Fukuta, Y.; Shirasaka, N.

Biosci. Biotechnol. Biochem.

82

2180-2190

750815

30836186

Characterization of a novel extracellular alpha-amylase from Ruminococcus bromii ATCC 27255 with neopullulanase-like activity

2019

Jung, J.H.; An, Y.K.; Son, S.Y.; Jeong, S.Y.; Seo, D.H.; Kim, M.K.; Park, C.S.

Int. J. Biol. Macromol.

130

605-614

752105

27108054

Purification and characterization of a novel intracellular alpha-amylase with a wide variety of substrates hydrolysis and transglycosylation activity from Paenibacillus sp. SSG-1

2018

Xu, Q.; Cao, Y.; Li, X.; Liu, L.; Qin, S.; Wang, Y.; Cao, Y.; Xu, H.; Qiao, D.

Protein Expr. Purif.

144

62-70

755942

27507216

Roles of N287 in catalysis and product formation of amylomaltase from Corynebacterium glutamicum

2016

Nimpiboon, P.; Krusong, K.; Kaulpiboon, J.; Kidokoro, S.; Pongsawasdi, P.

Biochem. Biophys. Res. Commun.

478

759-764

755955

28522291

Y418 in 410s loop is required for high transglucosylation activity and large-ring cyclodextrin production of amylomaltase from Corynebacterium glutamicum

2017

Tumhom, S.; Krusong, K.; Pongsawasdi, P.

Biochem. Biophys. Res. Commun.

488

516-521

756523

30563366

Current studies on the enzymatic preparation 2-O-alpha-D-glucopyranosyl-L-ascorbic acid with cyclodextrin glycosyltransferase

2019

Tao, X.; Su, L.; Wu, J.

Crit. Rev. Biotechnol.

39

249-257

759621

31838796

Carboxy-terminal region of a thermostable CITase from Thermoanaerobacter thermocopriae has the ability to produce long isomaltooligosaccharides

2019

Jeong, W.S.; Lee, Y.R.; Hong, S.J.; Choi, S.J.; Choi, J.H.; Park, S.Y.; Woo, E.J.; Kim, Y.M.; Park, B.R.

J. Microbiol. Biotechnol.

29

1938-1946

760023

28399167

Characterization of the Paenibacillus beijingensis DSM 24997 GtfD and its glucan polymer products representing a new glycoside hydrolase 70 subfamily of 4,6-alpha-glucanotransferase enzymes

2017

Gangoiti, J.; Lamothe, L.; van Leeuwen, S.S.; Vafiadi, C.; Dijkhuizen, L.

PLoS ONE

12

e0172622

764316

12092816

Cloning and sequencing of the genes encoding cyclic tetrasaccharide-synthesizing enzymes from Bacillus globisporus C11

2002

Aga, H.; Maruta, K.; Yamamoto, T.; Kubota, M.; Fukuda, S.; Kurimoto, M.; Tsujisaka, Y.

Biosci. Biotechnol. Biochem.

66

1057-1068